Interaction of serum albumin with various anionites

The interaction of bovine serum albumin (BSA) with the DEAE-Toyopearl (1), DEAE-Sepharose (2), silica gel coated with a polyethyleneimine layer cross- linked with diepoxide (PEI-silica gel) (3), and silica gel coated with a gr afted polyacrylamide layer with DEAE functionality (DEAE-PA-silica gel) (4) was studied. The ion-pair capacities of the sorbents with respect to picri c acid were determined. The binding of the proteins was studied under condi tions of frontal sorption (from solutions with a low ionic strength) and is ocratic elution. The data obtained were processed within the Framework of t he stoichiometric model of interaction of proteins and ionites. It was show n that the average number of charges participating in the binding of the pr oteins with the sorbents is large for sorbents (2) and (3) and small for so rbents (1) and (4), with the highest capacities of the chromatographic peak s of BSA under conditions of gradient elution being observed for sorbents ( 1) and (4). Electrophoresis in a polyacrylamide gel showed that the distrib utions of the components over the chromatographic fractions for the commerc ial BSA sample on sorbents(1) and (3) are similar.